IF2_STAAR
ID IF2_STAAR Reviewed; 705 AA.
AC Q6GHG6;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=SAR1245;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC -!- FUNCTION: One of the essential components for the initiation of protein
CC synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis
CC and promotes its binding to the 30S ribosomal subunits. Also involved
CC in the hydrolysis of GTP during the formation of the 70S ribosomal
CC complex. {ECO:0000255|HAMAP-Rule:MF_00100}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00100}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00100}.
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DR EMBL; BX571856; CAG40247.1; -; Genomic_DNA.
DR RefSeq; WP_000043642.1; NC_002952.2.
DR AlphaFoldDB; Q6GHG6; -.
DR SMR; Q6GHG6; -.
DR KEGG; sar:SAR1245; -.
DR HOGENOM; CLU_006301_5_1_9; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000596; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR Gene3D; 3.40.50.10050; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00100_B; IF_2_B; 1.
DR InterPro; IPR044145; IF2_II.
DR InterPro; IPR006847; IF2_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR000178; TF_IF2_bacterial-like.
DR InterPro; IPR015760; TIF_IF2.
DR InterPro; IPR023115; TIF_IF2_dom3.
DR InterPro; IPR036925; TIF_IF2_dom3_sf.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR PANTHER; PTHR43381; PTHR43381; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF04760; IF2_N; 2.
DR SUPFAM; SSF50447; SSF50447; 2.
DR SUPFAM; SSF52156; SSF52156; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00487; IF-2; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51722; G_TR_2; 1.
DR PROSITE; PS01176; IF2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis.
FT CHAIN 1..705
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137251"
FT DOMAIN 207..376
FT /note="tr-type G"
FT REGION 40..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..223
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 241..245
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 262..265
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 316..319
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 352..354
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 40..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 216..223
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 262..266
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 316..319
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 705 AA; 77830 MW; CAAC257FAE72D4C8 CRC64;
MSKQRIYEYA KELNLKSKEI IDELKSMNIE VSNHMQALED DQIKALDKKF KKEQKNDNKQ
STQNNHQKSN NQNQNKGQQK DNKKNQQQNN KGNKGNKKNN RNNKKNNKNN KPQSQPAAPK
EIPSKVTYQE GITVGEFADK LNVESSEIIK KLFLLGIVAN INQSLNQETI ELIADDYGVE
VEEEVVINEE DLSIYFEDEK DDPEAIERPA VVTIMGHVDH GKTTLLDSIR HTKVTAGEAG
GITQHIGAYQ IENDGKKITF LDTPGHAAFT TMRARGAQVT DITILVVAAD DGVMPQTIEA
INHAKEAEVP IIVAVNKIDK PTSNPDRVMQ ELTEYGLIPE DWGGETIFVP LSALSGDGID
DLLEMIGLVA EVQELKANPK NRAVGTVIEA ELDKSRGPSA SLLVQNGTLN VGDAIVVGNT
YGRIRAMVND LGQRIKTAGP STPVEITGIN DVPQAGDRFV VFSDEKQARR IGESRHEASI
VQQRQESKNV SLDNLFEQMK QGEMKDLNVI IKGDVQGSVE ALAASLMKID VEGVNVRIIH
TAVGAINESD VTLANASNGI IIGFNVRPDS GAKRAAEAEN VDMRLHRVIY NVIEEIESAM
KGLLDPEFEE QVIGQAEVRQ TFKVSKVGTI AGCYVTEGKI TRNAGVRIIR DGIVQYEGEL
DTLKRFKDDA KEVAKGYECG ITIENYNDLK EGDVIEAFEM VEIKR
